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関連する概念動画

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

7.0K
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

18.4K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.7K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
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Ligand-gated Ion Channels01:19

Ligand-gated Ion Channels

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Ligand-gated ion channels are transmembrane proteins with a channel for ions to pass through and a binding site for a ligand. The channel opens only when a ligand attaches to the binding site.
Three Subfamilies of Ligand-gated Ion Channels
Ligand-gated ion channels fall into three subfamilies. The 'Cys-loop' includes the nicotinic acetylcholine receptors, γ-aminobutyric acid (GABA), glycine, and 5-hydroxytryptamine receptors. The second one is the 'Pore-loop' channels that...
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Energy to Drive Translocation01:37

Energy to Drive Translocation

2.9K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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関連する実験動画

Updated: Feb 21, 2026

Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

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人間のTRPML1チャネル構造は,開いた形状と閉じた形状にある.

Philip Schmiege1,2, Michael Fine3, Günter Blobel1

  • 1Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10065, USA.

Nature
|October 12, 2017
PubMed
まとめ

研究者らは,閉じた状態と開いた状態のトランシーント受容体潜在性ムコリピン1 (TRPML1) チャンネルの構造を明らかにした. これは,カルシウムシグナル伝達,リソソーム機能,およびIV型粘脂症についての洞察を提供します.

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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy
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Expression and Purification of the Human Lipid-sensitive Cation Channel TRPC3 for Structural Determination by Single-particle Cryo-electron Microscopy

Published on: January 7, 2019

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Purification and Reconstitution of TRPV1 for Spectroscopic Analysis
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科学分野:

  • 構造生物学
  • 分子生物学
  • 細胞生物学

背景:

  • トランジエント・レセプター・ポテンシャル・ムコリピン1 (TRPML1) は,リソソムのカルシウムシグナル伝達とホメオスタシスに不可欠なカルシウム放出チャネルである.
  • TRPML1の機能障害は,重度の溶解体貯蔵障害である粘脂症型IVを引き起こします.

研究 の 目的:

  • 閉ざされた状態と開いた状態の両方で全長の人間のTRPML1の高解像度構造を決定する.
  • TRPML1チャネルの調節と活性化に伴う分子メカニズムを解明する.
  • IV型粘脂症の構造的基礎についての洞察を提供すること.

主な方法:

  • 電子冷凍顕微鏡 (cryo-EM) を使用して,ヒトのTRPML1の構造を得ました.
  • 構造はpH 7. 0でのアポ (閉じた) 状態とpH 6. 0でのアゴニスト結合 (開いた) 状態で決定された.

主要な成果:

  • 人間のTRPML1の2つの異なる冷凍-EM構造は,高解像度 (3. 72 Å と 3. 49 Å) で解像しました.
  • ヘリックスS5,S6およびポアヘリックス1で特定の残留物によって形成された独特の水害性穴は,アゴニスト結合部位として特定されました.
  • チャネルの開口は,下側のゲートの膨張と孔のヘリックス1の構造的シフトを含みます.

結論:

  • この研究は,TRPMLチャネルの規制メカニズムとその活性化プロセスを明らかにします.
  • この発見は,IV型粘脂症の病原性を分子的に理解することを可能にします.
  • この研究は,TRPチャネルの機能と規制の理解を進める.